ReviewMarine drugs2013
Protease inhibitors from marine venomous animals and their counterparts in terrestrial venomous animals.
Review in Marine drugs, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 103 citations in OpenAlex.
- Venom-Derived Enzyme Inhibitors as Anticancer Agents: Structure-Activity Relationships, Molecular Targets and Mechanistic Insights.Molecules (Basel, Switzerland) · 2026Review
- Conkazal-M1 from the MKAVA family of conotoxins: A dual-function protease inhibitor and neuroactive peptide.Protein science : a publication of the Protein Society · 2026Article
- Article
- Quantitative analysis of growth and diversification in venom data using database metrics.Database : the journal of biological databases and curation · 2026Article
- Discovery and Functional Characterization of Kunitz-Type Toxins from the Tetrodotoxin-Bearing Flatworm Planocera Multitencaculata.Marine biotechnology (New York, N.Y.) · 2026Article
- The green lacewing venom system and the complex mechanisms underlying its evolution.Molecular biology and evolution · 2026Article
- Structural similarities reveal an expansive conotoxin family with a two-finger toxin fold.Protein science : a publication of the Protein Society · 2025Article
- Molecular Insights into the Marine GastropodInternational journal of molecular sciences · 2025Article
- Proteomic Diversity of the Sea AnemoneMarine drugs · 2025Article
- Sea Anemone Kunitz Peptide HCIQ2c1: Structure, Modulation of TRPA1 Channel, and Suppression of Nociceptive Reaction In Vivo.Marine drugs · 2024Article
- Revealing the Diversity of Sequences, Structures, and Targets of Peptides from South China SeaMarine drugs · 2024Article
- Novel Niosome-Encapsulated 2,5-Diketopiperazine (BHPPD): Synthesis, Formulation, and Anti-breast Cancer Activity.Applied biochemistry and biotechnology · 2024Article
- Diversity analysis of sea anemone peptide toxins in different tissues of Heteractis crispa based on transcriptomics.Scientific reports · 2024Article
- RNAi-Mediated Suppression ofInternational journal of molecular sciences · 2024Article
- Venomous Noodles: The Evolution of Toxins in Nemertea through Positive Selection and Gene Duplication.Toxins · 2023Article
- Autophagy of Candida albicans cells after the action of earthworm Venetin-1 nanoparticle with protease inhibitor activity.Scientific reports · 2023Article
- Proteomic analyses of venom from a Spider Hawk,The journal of venomous animals and toxins including tropical diseases · 2023Article
- Molecular and Functional Characterization of a Novel Kunitz-Type Toxin-like Peptide in the Giant Triton SnailMarine drugs · 2022Article
- Kunitz-Type Peptides from Sea Anemones Protect Neuronal Cells against Parkinson's Disease Inductors via Inhibition of ROS Production and ATP-Induced P2X7 Receptor Activation.International journal of molecular sciences · 2022Article
- AsKC11, a Kunitz Peptide fromMarine drugs · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Kunitz-type protease inhibitors are the best-characterized family of serine protease inhibitors, probably due to their abundance in several organisms. These inhibitors consist of a chain of ~60 amino acid residues stabilized by three disulfide bridges, and was first observed in the bovine pancreatic trypsin inhibitor (BPTI)-like protease inhibitors, which strongly inhibit trypsin and chymotrypsin. In this review we present the protease inhibitors (PIs) described to date from marine venomous animals, such as from sea anemone extracts and Conus venom, as well as their counterparts in terrestrial venomous animals, such as snakes, scorpions, spiders, Anurans, and Hymenopterans. More emphasis was given to the Kunitz-type inhibitors, once they are found in all these organisms. Their biological sources, specificity against different proteases, and other molecular blanks (being also K+ channel blockers) are presented, followed by their molecular diversity. Whereas sea anemone, snakes and other venomous animals present mainly Kunitz-type inhibitors, PIs from Anurans present the major variety in structure length and number of Cys residues, with at least six distinguishable classes. A representative alignment of PIs from these venomous animals shows that, despite eventual differences in Cys assignment, the key-residues for the protease inhibitory activity in all of them occupy similar positions in primary sequence. The key-residues for the K+ channel blocking activity was also compared.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.